Abstract:
:The binding of cardiac glycosides to the E2 conformation of Na, K ATPase suggests that this conformation may represent a potential regulatory site for an endogenous ligand. To examine this hypothesis, delipidated and desalted, ethanolic extracts were prepared from plasma. Plasma extracts produced displacement of 3H-ouabain from Type I and II high affinity binding sites that was parallel to the displacement by cold ouabain. Plasma extracts shifted the binding curve of 3H-ouabain to the right indicating a competitive and reversible displacement. Extracts also produced a dose-dependent inhibition of Na, K ATPase and K-stimulated, p-nitrophenyl phosphatase activity. These results indicate that this ligand may function as an endogenous ligand to the E2 conformation of the Na, K ATPase molecule and be involved in its regulation.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Rauch AL,Buckalew VM Jrdoi
10.1016/0006-291x(88)90441-xsubject
Has Abstractpub_date
1988-01-29 00:00:00pages
648-54issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(88)90441-Xjournal_volume
150pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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更新日期:2010-03-19 00:00:00
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journal_title:Biochemical and biophysical research communications
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